Global low-frequency motions in protein allostery: CAP as a model system
Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP)...
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| Veröffentlicht in: | Biophysical reviews 2015, Vol.7 (2), p.175-182 |
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| container_title | Biophysical reviews |
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| creator | Townsend, Philip D. Rodgers, Thomas L. Pohl, Ehmke Wilson, Mark R. McLeish, Tom C. B. Cann, Martin J. |
| description | Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of
Escherichia coli
is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding. |
| doi_str_mv | 10.1007/s12551-015-0163-9 |
| format | Article |
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Escherichia coli
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Escherichia coli
is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.</description><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biological Techniques</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Cell Biology</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Nanotechnology</subject><subject>Review</subject><issn>1867-2450</issn><issn>1867-2469</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><recordid>eNpVkN1KAzEQhYMoVqsP4I3kBVbzvxsvhFK0FQp6odchTbJ1S3ZTk62yb29KtejAMMPMmQPzAXCF0Q1GqLxNmHCOC4R5TkELeQTOcCXKgjAhjw89RyNwntIaIcFIxU_BiAiUQ5AzMJ_5sNQe-vBV1NF9bF1nBtiGvgldgk0HNzH0LlftfUi9i8MdnE5eoE5QZ5l1HqYhz9sLcFJrn9zlTx2Dt8eH1-m8WDzPnqaTRbHBBMuiNtIxWxrsKl5RRpYltlZIg-uqdoSREnNKLEMWU8q4Lg3STtTGGYysFNbRMbjf-262y9ZZ47o-aq82sWl1HFTQjfq_6Zp3tQqfijFKEJbZ4PqvweHyl0kWkL0g5VW3clGtwzZ2-SmFkdqBV3vwKoNXO_BK0m8jMHTV</recordid><startdate>2015</startdate><enddate>2015</enddate><creator>Townsend, Philip D.</creator><creator>Rodgers, Thomas L.</creator><creator>Pohl, Ehmke</creator><creator>Wilson, Mark R.</creator><creator>McLeish, Tom C. B.</creator><creator>Cann, Martin J.</creator><general>Springer Berlin Heidelberg</general><scope>C6C</scope><scope>NPM</scope><scope>5PM</scope></search><sort><creationdate>2015</creationdate><title>Global low-frequency motions in protein allostery: CAP as a model system</title><author>Townsend, Philip D. ; Rodgers, Thomas L. ; Pohl, Ehmke ; Wilson, Mark R. ; McLeish, Tom C. B. ; Cann, Martin J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1219-fc9e4d7c1e858342b71dd69c1f8fe24271532d40d13345a7c0ae6fcec10d96de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biological Techniques</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Cell Biology</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Nanotechnology</topic><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Townsend, Philip D.</creatorcontrib><creatorcontrib>Rodgers, Thomas L.</creatorcontrib><creatorcontrib>Pohl, Ehmke</creatorcontrib><creatorcontrib>Wilson, Mark R.</creatorcontrib><creatorcontrib>McLeish, Tom C. B.</creatorcontrib><creatorcontrib>Cann, Martin J.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>PubMed</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical reviews</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Townsend, Philip D.</au><au>Rodgers, Thomas L.</au><au>Pohl, Ehmke</au><au>Wilson, Mark R.</au><au>McLeish, Tom C. B.</au><au>Cann, Martin J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Global low-frequency motions in protein allostery: CAP as a model system</atitle><jtitle>Biophysical reviews</jtitle><stitle>Biophys Rev</stitle><addtitle>Biophys Rev</addtitle><date>2015</date><risdate>2015</risdate><volume>7</volume><issue>2</issue><spage>175</spage><epage>182</epage><pages>175-182</pages><issn>1867-2450</issn><eissn>1867-2469</eissn><abstract>Allostery is a fundamental process by which ligand binding to a protein alters its activity at a distant site. There is considerable evidence that allosteric cooperativity can be communicated by the modulation of protein dynamics without conformational change. The Catabolite Activator Protein (CAP) of
Escherichia coli
is an important experimental exemplar for entropically driven allostery. Here we discuss recent experimentally supported theoretical analysis that highlights the role of global low-frequency dynamics in allostery in CAP and identify how allostery arises as a natural consequence of changes in global low-frequency protein fluctuations on ligand binding.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>26000062</pmid><doi>10.1007/s12551-015-0163-9</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry Biological and Medical Physics Biological Techniques Biomedical and Life Sciences Biophysics Cell Biology Life Sciences Membrane Biology Nanotechnology Review |
| title | Global low-frequency motions in protein allostery: CAP as a model system |
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